Information on EC 1.5.1.34 - 6,7-dihydropteridine reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.5.1.34
-
RECOMMENDED NAME
GeneOntology No.
6,7-dihydropteridine reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H + H+
show the reaction diagram
-
-
-
-
a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H + H+
show the reaction diagram
ordered bi-bi mechanism, binding of NADH first and dissociation of NAD+ last
-
a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H + H+
show the reaction diagram
structural and mechanistic characteristics
-
a 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H + H+
show the reaction diagram
catalytic triad consists of Y182, K186, and D169
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Folate biosynthesis
-
-
L-phenylalanine degradation V
-
-
Metabolic pathways
-
-
phenylalanine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase
The substrate is the quinonoid form of dihydropteridine. Not identical with EC 1.5.1.3 dihydrofolate reductase.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DHPR
-
-
-
-
dihydropteridine reductase (NADH)
-
-
-
-
NADH-dihydropteridine reductase
-
-
-
-
NADPH-dihydropteridine reductase
-
-
-
-
NADPH-specific dihydropteridine reductase
-
-
-
-
reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
70851-99-9
-
9074-11-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
activity is reduced in patients with haematological malignancies
-
-
Manually annotated by BRENDA team
enzyme from liver, fibroblast cultures and continous lymphoid cells shows identical antigenic properties
-
-
Manually annotated by BRENDA team
patients from Calabria, Italy, one patient with traces of activity, two patients without activity
-
-
Manually annotated by BRENDA team
patients with vitiligo
Uniprot
Manually annotated by BRENDA team
sp. ATCC 11299a
-
-
Manually annotated by BRENDA team
multiple forms: I, II, II
-
-
Manually annotated by BRENDA team
rapid increase of enzyme level during development
-
-
Manually annotated by BRENDA team
spontaneously hypertensive rats of various ages and age-matched normotensive Wistar-Kyoto rats
-
-
Manually annotated by BRENDA team
strain HB27, gene DHTt
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
the brain stem of intrauterine growth-restricted offspring show significant increase of L-tryptophan, 5-hydroxytryptamine, tryptophan-5-hydroxylase and also dihydropteridine activity in the brain stem in comparison to controls. Intrauterine growth restriction produces an increase of serotonin biosynthesis in the brain stem. This is accompanied by an increase in dihydropteridine activity that appears to be a compensatory mechanism to maintain sufficient tetrahydrobiopterin for the donation of electrons during the accelerated synthesis of brain serotonin in intrauterine growth-restricted rats
malfunction
-
enzyme inhibition results in a significant increase in transforming growth factor-beta1 expression
metabolism
-
enzyme catalyzes the last step of tetrahydrobiopterin recycling
physiological function
-
enzyme in the regeneration pathway of tetrahydrobiopterin, expression is reduced in hypertensive rats compared to normotensive rats, tetrahydrobiopterin levels are attenuated in hypertensive rat aortic smooth muscle, tetrahydrobiopterin inhibits a serotonin-mediated vascular contraction increase
physiological function
-
the enzyme is an important factor mediating diabetic nephropathy through its regulation of transforming growth factor-beta1/Smad3 signaling and NADPH oxidase
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(6R)-L-erythro-dihydrobiopterin + NADH + H+
?
show the reaction diagram
Q86A17
-
-
-
?
(6R)-tetrahydrobiopterin + NAD(P)+
?
show the reaction diagram
Q8WTJ2
-
-
-
r
(6R,S)-6-hydroxy-methyltetrahydropterin + NAD(P)+
?
show the reaction diagram
Q8WTJ2
low activity
-
-
r
(6R,S)-6-methyl-tetrahydropterin + NAD(P)+
?
show the reaction diagram
Q8WTJ2
low activity
-
-
r
(6R,S)-tetrahydrodictyopterin + NAD(P)+
?
show the reaction diagram
Q8WTJ2
-
-
-
r
(6R,S)-tetrahydrofolic acid + NAD(P)+
?
show the reaction diagram
Q8WTJ2
low activity
-
-
r
(6R,S)-tetrahydroneopterin + NAD(P)+
?
show the reaction diagram
Q8WTJ2
low activity
-
-
r
(6S)-tetrahydrobiopterin + NAD(P)+
?
show the reaction diagram
Q8WTJ2
low activity
-
-
r
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
show the reaction diagram
-
-
-
-
-
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
show the reaction diagram
-
-
-
?
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
show the reaction diagram
-
-
-
?
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
show the reaction diagram
-
NADH is 20fold more effective than NADPH
-
?
2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine + NAD(P)+
show the reaction diagram
-
3% activity with NADPH
-
?
2-amino-4-hydroxy-6-methyl-5,6,7,8-tetrahydropteridine + NADH
?
show the reaction diagram
-
-
-
-
?
2-amino-4-hydroxy-6-methyl-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-6-methyl-tetrahydropteridine + NAD(P)+
show the reaction diagram
-
-
-
?
2-amino-4-hydroxy-7-methyl-dihydropteridine + NAD(P)H
2-amino-4-hydroxy-7-methyl-tetrahydropteridine + NAD(P)+
show the reaction diagram
-
-
-
?
5,6,7,8-tetrahydropteridine + NAD(P)+
6,7-dihydropteridine + NAD(P)H
show the reaction diagram
Q8WTJ2
enzyme is required for recycling of 6,7-dihydropteridine, in vivo regulation is related to growth phase
-
-
r
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
-
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
P09417
last step of recycling of the cofactor (6R)-L-erythro-5,6,7,8-tetrahydrobiopteridine essential for aromatic amino acid hydroxylases and nitric oxide synthases, regulatory mechanism involve H2O2, enzyme inactivation because of H2O2 accumulation in the epidermis contributes to the pathomechanism of vitiligo
-
-
?
6,7-dimethyl-7,8-dihydropteridine + NADPH
(6R)-L-erythro-6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + NADP+
show the reaction diagram
-
-
-
-
?
6,7-dimethyl-7,8-dihydropteridine + NADPH
(6R)-L-erythro-6,7-dimethyl-5,6,7,8-tetrahydrobiopterin + NADP+
show the reaction diagram
-
-
-
-
-
6,7-dimethyl-7,8-dihydropterin + NADPH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
show the reaction diagram
-
-
-
-
-
6,7-dimethyl-7,8-dihydropterin + NADPH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
show the reaction diagram
-
-
-
-
-
6,7-dimethyl-7,8-dihydropterin + NADPH + H+
6,7-dimethyl-5,6,7,8-tetrahydropterin + NADP+
show the reaction diagram
-
as the quinonoid forms of pterines are very unstable, the reaction is carried out with a dimethyl analogue in the presence of H2O2 and radish peroxidase to allow the continuous formation of 6,7-dimethyl-7,8-dihydropterine, activity is 25fold higher than the nitroreductase activity 2,4-dinitrophenol
-
-
?
6,7-dimethyl-tetrahydropterin + NAD(P)+
?
show the reaction diagram
Q8WTJ2
low activity
-
-
r
6,7-dimethyldihydropterin + NADH + H+
6,7-dimethyltetrahydropterin + NAD+
show the reaction diagram
Q86A17
-
-
-
?
dihydrobiopterin + NADH + H+
tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
-
dihydrobiopterin + NADH + H+
tetrahydrobiopterin + NAD+
show the reaction diagram
-
pH 7.4, 37C
-
-
?
dihydrofolate + NADPH
tetrahydrofolate + NADP+
show the reaction diagram
-
-
-
-
?
dihydropteroic acid + NAD(P)H
tetrahydropteroate + NAD(P)+
show the reaction diagram
-
-
-
?
dihydropteroylglutamic acid + NAD(P)H
tetrahydropteroylglutamate + NAD(P)+
show the reaction diagram
-
-
-
?
quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
-
-
-
-
quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
-
-
-
-
quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
specific for NADH
-
?
quinoid dihydrobiopterin + NAD(P)H
tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
NADH is 2.5fold more effective than NADPH
-
?
quinonoid (6R)-D-threo-dihydrobiopterin + NADH + H+
?
show the reaction diagram
Q86A17
-
-
-
?
quinonoid 6,6-dimethyldihydropterin + NAD(P)H
6,6-dimethyltetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
-
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
enzyme from adrenal medulla
-
?
quinonoid 6,7-dimethyl-7,8-(6H)-dihydropterin + NAD(P)H
6,7-dimethyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
no activity with 6,6,8-trimethyl-7,8-(6H)-dihydropterin
-
-
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
-
-
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
-
-
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 6-methyl-7,8-(6H)-dihydropterin + NAD(P)H
6-methyl-5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
NADPH-specific enzyme from liver, NADPH is 660times more effective than NADH
-
-
-
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
more specific for NADH, 50% activity with NADPH, no activity with biopterin and 7,8-dihydrobiopterin
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
enzyme also has pterin-independent NADH and NADPH oxidoreductase activity with potassium ferricyanide
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
enzyme prefers NADH
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydropterin + NAD(P)+
show the reaction diagram
-
absolutely specific for quinonoid dihydro-isomer corresponding to 7,8-dihydropterins
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
-
-
-
-
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
-
-
-
-
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
-
-
-
-
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
may also have an important role in regulation of catecholamine synthesis
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
no marked specificity for the pteridine cofactor that occurs naturally in this organism L-threo-neopterin
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan
-
-
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
essential component of catecholamine biosynthetic metabolism
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
essential component of the hepatic phenylalanine hydroxylating system
-
?
quinonoid dihydro-2-methylamino-4-hydroxy-6,7-dimethylpteridine + NAD(P)H
tetrahydro-2-methylamino-4-hydroxy-6,7-dimethylpteridine + NAD(P)+
show the reaction diagram
-
approx. one-third of activity with 2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropterid
-
?
quinonoid dihydro-L-threo-neopterin + NAD(P)H
tetrahydro-L-threo-neopterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
-
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
-
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
-
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
-
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
-
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
-
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
?
quinonoid dihydromonapterin + NAD(P)H
tetrahydromonapterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid dihydroneopterin + NAD(P)H
tetrahydroneopterin + NAD(P)+
show the reaction diagram
-
-
-
?
K3Fe(CN)6 + NAD(P)H
K4Fe(CN)6 + NAD(P)+
show the reaction diagram
-
-
-
?
additional information
?
-
-
no activity with potassium ferricyanide, 6-biopterin, and 6-methyl-7,8-dihydropterine
-
-
-
additional information
?
-
Q8WTJ2
substrate specificity, enzyme shows selectivity for pterin substrates with a 6-(1', 2'-dihydroxypropyl) substitution
-
-
-
additional information
?
-
-
essential part of the hydroxylating system of the aromatic amino acids phenylalanine, tyrosine and tryptophan, reduces quinonoid dihydropterine to regenerate tetrahydrobiopterin, main metabolic derangements caused by DHPR deficiency are hyperphenylalaninaemia and impaired production of the monoamine neurotransmitters dopamine, noradrenaline and serotonin, DHPR deficiency patients can develop severe and progressive neurological damage
-
-
-
additional information
?
-
-
in vivo role as dihydropteridine reductase involved in aromatic amino acids metabolism suggested, enzyme shows nitroreductase activity with several different substrates such as 2,4-dinitrophenol, 2,4-dinitrobenzoate and nitrofurazone
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,6,7,8-tetrahydropteridine + NAD(P)+
6,7-dihydropteridine + NAD(P)H
show the reaction diagram
Q8WTJ2
enzyme is required for recycling of 6,7-dihydropteridine, in vivo regulation is related to growth phase
-
-
r
6,7-dihydropteridine + NADH
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
P09417
last step of recycling of the cofactor (6R)-L-erythro-5,6,7,8-tetrahydrobiopteridine essential for aromatic amino acid hydroxylases and nitric oxide synthases, regulatory mechanism involve H2O2, enzyme inactivation because of H2O2 accumulation in the epidermis contributes to the pathomechanism of vitiligo
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
-
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
may also have an important role in regulation of catecholamine synthesis
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
no marked specificity for the pteridine cofactor that occurs naturally in this organism L-threo-neopterin
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan
-
-
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
essential enzyme component of the complex system catalyzing hydroxylation of phenylalanine, tyrosine and tryptophan
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
essential component of catecholamine biosynthetic metabolism
-
?
quinonoid 7,8-(6H)-dihydrobiopterin + NAD(P)H
5,6,7,8-tetrahydrobiopterin + NAD(P)+
show the reaction diagram
-
essential component of the hepatic phenylalanine hydroxylating system
-
?
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
?
dihydrobiopterin + NADH + H+
tetrahydrobiopterin + NAD+
show the reaction diagram
-
pH 7.4, 37C
-
-
?
additional information
?
-
-
essential part of the hydroxylating system of the aromatic amino acids phenylalanine, tyrosine and tryptophan, reduces quinonoid dihydropterine to regenerate tetrahydrobiopterin, main metabolic derangements caused by DHPR deficiency are hyperphenylalaninaemia and impaired production of the monoamine neurotransmitters dopamine, noradrenaline and serotonin, DHPR deficiency patients can develop severe and progressive neurological damage
-
-
-
additional information
?
-
-
in vivo role as dihydropteridine reductase involved in aromatic amino acids metabolism suggested
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
contains bound FAD
NAD(P)H
Q8WTJ2
NADH is the preferred cofactor
NADH
-
enzyme prefers NADH; liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH; utilizes both NADH and NADPH
NADH
-
enzyme prefers NADH
NADH
-
enzyme binds 1 mol NADH per mol enzyme; enzyme prefers NADH
NADH
-
utilizes both NADH and NADPH
NADH
-
enzyme prefers NADH; utilizes both NADH and NADPH
NADH
-
enzyme prefers NADH; utilizes both NADH and NADPH
NADH
-
enzyme prefers NADH; utilizes both NADH and NADPH
NADH
-
enzyme prefers NADH; utilizes both NADH and NADPH
NADH
-
enzyme prefers NADH; utilizes both NADH and NADPH
NADH
-
utilizes both NADH and NADPH
NADH
-
utilizes both NADH and NADPH
NADH
-
liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH
NADPH
-
liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH; NADH is preferred; utilizes both NADH and NADPH
NADPH
-
inactive with NADPH, specific for NADPH; NADH is preferred
NADPH
-
NADH is preferred
NADPH
-
utilizes both NADH and NADPH
NADPH
-
NADH is preferred; utilizes both NADH and NADPH
NADPH
-
NADH is preferred; utilizes both NADH and NADPH
NADPH
-
NADH is preferred; utilizes both NADH and NADPH
NADPH
-
NADH is preferred; utilizes both NADH and NADPH
NADPH
-
NADH is preferred; utilizes both NADH and NADPH
NADPH
-
utilizes both NADH and NADPH
NADPH
-
utilizes both NADH and NADPH
NADPH
-
-
NADPH
-
liver: 2 distinct dihydropteridine reductases which catalyze the conversion of the quinonoid dihydropteridine to tetrahydropterin: NADH-dihydropteridine reductase, DPR, utilizes NADH as a better substrate than NADPH, NADPH-specific dihydropteridine reductase, TPR, shows strict specificity for NADPH
FMN
-
one molecule bound per enzyme
additional information
-
no flavin prosthetic group
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-2,10,11-trihydroxy-N-n-propylaporphine
-
0.0017 mM, 50% inhibition
(R)-2,10,11-trihydroxy-N-n-propylaporphine
-
0.0016 mM, 50% inhibition
(R)-2,10,11-trihydroxyaporphine
-
0.0016 mM, 50% inhibition
(R)-2,10,11-trihydroxyaporphine
-
0.0007 mM, 50% inhibition
(R)-2,11-dihydroxy-10-methoxy-aporphine
-
0.013 mM, 50% inhibition
(R)-2,11-dihydroxy-10-methoxy-aporphine
-
0.016 mM, 50% inhibition
(R)-apocodeine
-
0.079 mM, 50% inhibition
(R)-apocodeine
-
0.087 mM, 50% inhibition
(R)-apomorphine
-
0.002 mM, 50% inhibition
(R)-apomorphine
-
0.0012 mM, 50% inhibition
(R)-N-chloroethylnorapomorphine
-
0.0029 mM, 50% inhibition
(R)-N-hydroxyethylnorapomorphine
-
0.001 mM, 50% inhibition
(R)-N-hydroxyethylnorapomorphine
-
0.0013 mM, 50% inhibition
(R)-N-n-propylaporphine
-
-
(R)-N-n-propylnorapomorphine
-
0.0018 mM, 50% inhibition
(R)-N-n-propylnorapomorphine
-
0.0017 mM, 50% inhibition
(R)-norapomorphine
-
0.0028 mM, 50% inhibition
(R)-norapomorphine
-
0.0014 mM, 50% inhibition
(S)-2,10,11-trihydroxyaporphine
-
0.0015 mM, 50% inhibition
(S)-2,10,11-trihydroxyaporphine
-
0.0014 mM, 50% inhibition
(S)-bulbocapnine
-
0.148 mM, 50% inhibition
(S)-bulbocapnine
-
0.151 mM, 50% inhibition
(S)-N-n-propylnorapomorphine
-
0.0022 mM, 50% inhibition
(S)-N-n-propylnorapomorphine
-
0.0018 mM, 50% inhibition
1-methyl-4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0034 mM, 50% inhibition
1-methyl-4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
1-methyl-4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0093 mM, 50% inhibition
1-methyl-4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
1-methyl-4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
-
0.27 mM, 50% inhibition
1-methyl-4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
-
-
1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.003 mM, 50% inhibition
1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
0.3 mM, 50% inhibition
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
-
2,4-diamino-7,8-dihydropteroylglutamic acid
-
-
2,4-Diaminopteridine
-
-
2,4-diaminopteroic acid
-
-
2,4-diaminopteroylglutamic acid
-
-
2,6-dichlorophenolindophenol
-
0.0001 mM, 50% inhibition
2,6-dichlorophenolindophenol
-
inhibition of NADPH-specific enzyme
3',4'-deoxynorlaudanosolinecarboxylic acid
-
noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine and NADH
3(4-hydroxyphenyl)pyruvate
-
0.0033 mM, 50% inhibition
3(4-hydroxyphenyl)pyruvate
-
0.0044 mM, 50% inhibition
3-iodotyrosine
-
weak inhibition
3-O-methyldopamine
-
0.06 mM, 50% inhibition
3-O-Methylepinephrine
-
0.18 mM, 50% inhibition
3-phenylpyruvic acid
-
4.7 mM, 50% inhibition
3-phenylpyruvic acid
-
5.9 mM, 50% inhibition
4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0036 mM, 50% inhibition
4-(3',4'-dihydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0072 mM, 50% inhibition
4-(3'-methoxy-4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
-
0.34 mM, 50% inhibition
4-(4'-chlorophenyl)-1,2,3,6-tetrahydropyridine
-
-
4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
0.0059 mM, 50% inhibition
4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
-
4-hydroxyphenyllactate
-
0.058 mM, 50% inhibition
4-hydroxyphenyllactate
-
0.071 mM, 50% inhibition
4-O-Methyldopamine
-
0.069 mM, 50% inhibition
4-phenyl-1,2,3,6-tetrahydropyridine
-
12 mM, 50% inhibition
4-phenyl-1,2,3,6-tetrahydropyridine
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
0.57 mM, 98% inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
no inactivation in the presence of NADH
5,5'-dithiobis(2-nitrobenzoate)
-
0.1 mM, 60% inhibition
5-Hydroxydopamine
-
0.042 mM, 50% inhibition
6-Hydroxydopamine
-
0.029 mM, 50% inhibition
Adrenochrome
-
-
alpha-Methyltyrosine
-
1.1 mM, 50% inhibition
aminochrome
-
oxidation product of adrenaline, competitive vs. NADH
aminopterin
-
-
aminopterin
-
1 mM, 50% inhibition, NADPH-specific enzyme
aminopterin
-
competitive vs. 2-amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine
aminopterin
-
-
aminopterin
-
no inhibition up to 0.1 mM
aminopterin
-
1 mM, 50% inhibition
aminopterin
-
0.025 mM, 50% inhibition of NADH-specific enzyme, 1 mM, 50% inhibition of NADPH-specific enzyme
catecholamine
-
-
CdCl2
-
0.1 mM, complete inactivation
cis-Diaminodichloroplatinum
-
-
CoCl2
-
0.01 mM, 30% inhibition
dopachrome
-
0.6 mM, 50% inhibition
dopamine
-
0.1 mM, 50% inhibition
dopamine
-
no inhibition below 0.2 mM
dopamine
-
-
dopamine
-
noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
epinephrine
-
0.13 mM, 50% inhibition
H2O2
P09417
regulatory function in vivo, above 0.03 mM, oxidation of Met146 and Met151 leads to inactivation of the enzyme due to disruption of the NADH-binding site
HgCl2
-
0.002 mM, 50% inhibition, enzyme from brain
HgCl2
-
0.0001 mM, 60% inhibition
higenamine
-
noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine and NADH
higenamine-1-carboxylic acid
-
noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
iodoacetamide
-
-
K2PtCl4
-
0.208 mM, half-life of inactivation: 3.1 min, NADH and 2 mM dithiothreitol completely protect
L-beta-3,4-dihydroxyphenylalanine
-
0.23 mM, 50% inhibition
L-beta-3,4-dihydroxyphenylalanine
-
trivial name L-DOPA, 0.34 mM, 50% inhibition
L-beta-3,4-dihydroxyphenylalanine
-
0.02 mM, 50% inhibition
L-beta-3,4-dihydroxyphenylalanine
-
0.8 mM, 50% inhibition after 3 h, 80% inhibition after 16 h due to oxidation of L-DOPA to dopachrome which inhibits the enzyme
L-thyroxine
-
mixed-type inhibition
L-tyrosine
-
noncompetitive vs. NADPH
L-tyrosine
-
; 0.61 mM, 50% inhibition
L-tyrosine
-
; 0.44 mM, 50% inhibition
m-tyramine
-
0.036 mM, 50% inhibition
m-tyramine
-
0.044 mM, 50% inhibition
methopterin
-
0.038 mM, 50% inhibition of NADH-specific enzyme
methopterin
-
0.7 mM, 50% inhibition of NADPH-specific enzyme
methopterin
-
1 mM, 10% inhibition
methopterin
-
0.038 mM, 50% inhibition of NADH-specific enzyme; 0.7 mM, 50% inhibition of NADPH-specific enzyme
methotrexate
-
no inhibition up to 0.1 mM
methotrexate
-
-
methotrexate
-
competitive vs. quinoid 6-methyl-7,8-dihydropterin
methotrexate
-
-
MgCl2
-
0.1 mM, complete inactivation
N-bromosuccinimide
-
-
N-ethylmaleimide
-
5 mM, complete inhibition of reduced enzyme
N-ethylmaleimide
-
1 mM, 76% inhibition
N-Methyldopamine
-
0.027 mM, 50% inhibition
NAD+
-
competitive vs. NADH
NADP+
-
competitive vs. NADPH
NADP+
-
; competitive vs. NADPH
Noradrenalin
-
-
Noradrenalin
-
no inhibition below 0.2 mM
noradrenaline
-
-
norepinephrine
-
0.2 mM, 50% inhibition
o-hydroxyphenylacetic acid
-
6.9 mM, 50% inhibition
o-hydroxyphenylacetic acid
-
8.1 mM, 50% inhibition
Octopamine
-
0.19 mM, 50% inhibition
p-chloromercuribenzoate
-
0.2 mM, 50% inhibition, enzyme from brain
p-chloromercuribenzoate
-
0.4 mM, 50% inhibition
p-chloromercuribenzoate
-
complete inactivation at inhibitor/enzyme ratios greater than 6/1, NADH protects
p-chloromercuribenzoate
-
0.01 mM, 70% inhibition
phenylacetic acid
-
6.6 mM, 50% inhibition
phenylacetic acid
-
6.9 mM, 50% inhibition
phenylalanine
-
-
Phenyllactate
-
-
phenylpyruvate
-
-
phenylpyruvate
-
-
quinonoid 2,4-diamino-7,8-dihydropteroylglutamic acid
-
-
quinonoid 6,6,8-trimethyl-7,8-dihydro(6H)pterin
-
0.2 mM, 50% inhibition
quiononoid 2,4-diamino-7,8-dihydropteroylglutamic acid
-
-
salsolinol
-
noncompetitive vs. quinoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
serotonin
-
-
tetrahydrobiopterin
-
above 0.05 mM, substrate inhibition
trans-Diaminodichloroplatinum
-
-
trans-Pt(NH3)Cl2
-
1 mM, 96% inactivation after 2 h
tryptophan
-
-
tyramine
-
0.04 mM, 50% inhibition
tyramine
-
0.046 mM, 50% inhibition
tyramine
-
IC50: 0.04 mM
[4-hydroxyphenyl]acetic acid
-
-
MnCl2
-
0.1 mM, complete inactivation
additional information
-
quinone products of L-DOPA oxidation are responsible for the time-dependent inactivation of the enzyme
-
additional information
-
enzyme from adrenal medulla, not inhibited by aminopterin and methotrexate
-
additional information
-
not inhibited by EDTA, o-phenanthroline, and 2,2'-bipyridyl
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.036
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydro-pteridine
-
37C, pH 7.2
0.036
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine
-
-
0.34
2-Amino-4-hydroxy-6,7-dimethyl-quinonoid-dihydropteridine
-
-
0.0152
2-amino-4-hydroxy-6,7-dimethyldihydropteridine
-
cofactor NADH
-
0.017
5,6,7,8-tetrahydrobiopterin
-
37C, pH 7.2
0.0063
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
cofactor NADPH
0.0152
6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
-
cofactor NADH
0.012
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
-
0.015
6,7-dimethyl-5,6,7,8-tetrahydropterin
-
-
0.03
6,7-dimethyldihydropterin
-
-
0.035
6-Methyl-dihydropterin
-
-
0.366
6-methyl-quinonoid 7,8-(6H)-dihydropterin
-
-
0.0014
6-methyl-tetrahydropterin
-
NADPH-specific liver enzyme, cofactor NADPH
0.0056
6-methyl-tetrahydropterin
-
NADH-specific liver enzyme, cofactor NADH
0.0058
6-methyl-tetrahydropterin
-
NADH-specific liver enzyme, cofactor NADPH
0.013
6-methyl-tetrahydropterin
-
NADPH-specific liver enzyme, cofactor NADH
0.03
6-methyldihydropterin
-
-
0.16
biopterin
-
-
0.754
cis-6,7-dimethyl-quinonoid 7,8-(6H)-dihydropterin
-
-
0.004
dihydrobiopterin
-
-
1.45
L-threo-neopterin
-
-
0.00079
NADH
-
reduction of quinonoid 7,8-dihydro-6-methylpterin
0.00085
NADH
-
; NADH-specific liver enzyme
0.0015
NADH
-
reduction of quinonoid 7,8-dihydrobiopterin
0.0015
NADH
-
NADH-specific liver enzyme, substrate tetrahydrobiopterin
0.002
NADH
-
recombinant Y150K glutathione-S-transferase fusion mutant enzyme; recombinant Y150S glutathione-S-transferase fusion mutant enzyme
0.002
NADH
-
Y146F/A133S mutant enzyme
0.0022
NADH
-
-
0.0024
NADH
-
recombinant Y150F mutant enzyme
0.0028
NADH
-
-
0.003
NADH
-
Y146F mutant enzyme
0.0037
NADH
-
enzyme form III
0.004
NADH
-
reduction of quinonoid dihydrobiopterin
0.004
NADH
-
substrate tetrahydrobiopterin
0.0043
NADH
-
recombinant Y150H mutant enzyme
0.0044
NADH
-
recombinant Y150E glutathione-S-transferase fusion mutant enzyme
0.00441
NADH
-
enzyme form II
0.0047
NADH
-
-
0.0049
NADH
-
recombinant Y150S mutant enzyme
0.005
NADH
-
recombinant Y150F glutathione-S-transferase fusion mutant enzyme
0.0055
NADH
-
enzyme form I
0.0057
NADH
-
reduction of quinonoid 2-amino-4-hydroxy-6,7-dimetyldihydropteridine
0.0057
NADH
-
substrate 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
0.0059
NADH
-
recombinant Y150H glutathione-S-transferase fusion mutant enzyme
0.0064
NADH
-
recombinant Y150E mutant enzyme
0.008
NADH
-
-
0.008
NADH
-
Y146H mutant enzyme
0.009
NADH
-
recombinant enzyme
0.01
NADH
-
Y146F mutant enzyme
0.0114
NADH
-
recombinant wild-type glutathione-S-transferase fusion enzyme
0.012
NADH
-
W86I mutant enzyme
0.013
NADH
-
native liver enzyme
0.013
NADH
-
recombinant wild-type enzyme
0.013
NADH
-
K150E mutant enzyme; recombinant wild-type enzyme
0.013
NADH
-
-
0.017
NADH
-
A6V mutant enzyme
0.017
NADH
-
Y146H mutant enzyme
0.0172
NADH
-
recombinant wild-type enzyme
0.021
NADH
-
recombinant liver enzyme
0.021
NADH
-
K150I mutant enzyme
0.022
NADH
-
enzyme from brain
0.022
NADH
-
A133S mutant enzyme
0.025
NADH
-
A133S mutant enzyme
0.027
NADH
-
W104F mutant enzyme
0.027
NADH
-
Y146F/K150Q double mutant enzyme
0.029
NADH
-
-
0.029
NADH
-
-
0.029
NADH
-
K150Q mutant enzyme
0.036
NADH
-
D37I mutant enzyme
0.04651
NADH
Q86A17
apparent value, in 50 mM Tris-HCl, pH 7.5, at 25C
0.074
NADH
-
NADH specific liver enzyme, substrate tetrahydrobiopterin
0.091
NADH
-
-
0.2
NADH
-
recombinant G23D mutant enzyme
0.276
NADH
-
recombinant G151S mutant enzyme
0.77
NADH
-
37C, pH 7.2
2.9
NADH
-
reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme
2.9
NADH
-
NADPH specific liver enzyme, substrate 6-methyltetrahydropterin
0.0014
NADPH
-
reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme
0.0014
NADPH
-
NADPH specific liver enzyme, substrate 6-methyl-tetrahydropterin
0.0017
NADPH
-
reduction of quinonoid 7,8-dihydropterin, NADPH-specific enzyme
0.0017
NADPH
-
NADPH specific liver enzyme, substrate tetrahydrobiopterin
0.0088
NADPH
-
-
0.029
NADPH
-
37C, pH 7.2
0.0709
NADPH
-
reduction of quinonoid dihydrobiopterin
0.0709
NADPH
-
substrate tetrahydrobiopterin
0.074
NADPH
-
reduction of quinonoid 7,8-dihydrobiopterin
0.076
NADPH
-
NADH-specific liver enzyme
0.08
NADPH
-
reduction of quinonoid 2-amino-4-hydroxy-6,7-dimethyldihydropteridine
0.0806
NADPH
-
substrate 6,7-dimethyl-5,6,7,8-tetrahydrobiopterin
0.095
NADPH
-
reduction of quinonoid 7,8-dihydrobiopterin
0.095
NADPH
-
NADH specific liver enzyme, substrate 6-methyl-tetrahydropterin
0.1
NADPH
-
-
0.11
NADPH
-
-
0.135
NADPH
-
recombinant enzyme
0.29
NADPH
-
-
0.5
NADPH
-
-
0.77
NADPH
-
-
0.018
quinonoid 2-amino-4-hydroxy-6,7-dimethyl-7,8-dihydropteridine
-
recombinant enzyme
0.006
quinonoid 2-amino-4-hydroxy-6,7-dimethyldihydropteridine
-
cofactor NADPH
0.34
quinonoid 2-amino-4-hydroxy-6,7-dimethyldihydropteridine
-
-
0.4
Quinonoid 6,6-dimethyldihydropterin
-
-
0.008
quinonoid 6,7-dimethyldihydropteridine
-
A133S mutant enzyme
0.027
quinonoid 6,7-dimethyldihydropteridine
-
recombinant wild-type enzyme
0.1
quinonoid 6,7-dimethyldihydropteridine
-
Y146F/A133S mutant enzyme
0.17
quinonoid 6,7-dimethyldihydropteridine
-
Y146H mutant enzyme
0.29
quinonoid 6,7-dimethyldihydropteridine
-
K150E mutant enzyme
0.46
quinonoid 6,7-dimethyldihydropteridine
-
Y146F mutant enzyme
0.0008
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 20C
0.0015
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 25C
0.0024
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 30C
0.0063
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 37C
0.669
quinonoid 7,8-(6H)-dihydropterin
-
-
0.0014
quinonoid 7,8-dihydro-6-methylpterin
-
cofactor NADPH, NADPH-specific enzyme
0.0056
quinonoid 7,8-dihydro-6-methylpterin
-
cofactor NADH
0.0058
quinonoid 7,8-dihydro-6-methylpterin
-
cofactor NADPH
0.013
quinonoid 7,8-dihydro-6-methylpterin
-
cofactor NADH, NADPH-specific enzyme
0.00015
quinonoid 7,8-dihydrobiopterin
-
recombinant enzyme
0.0011
quinonoid 7,8-dihydrobiopterin
-
cofactor NADPH
0.0016
quinonoid 7,8-dihydrobiopterin
-
cofactor NADH
0.0068
quinonoid 7,8-dihydropterin
-
cofactor NADPH, NADPH-specific enzyme
0.01
quinonoid dihydro-6,7-dimethyldihydropterin
-
enzyme from brain
-
0.028
quinonoid dihydrobiobiopterin
-
K150E mutant enzyme
0.00032
quinonoid dihydrobiopterin
-
-
0.0004
quinonoid dihydrobiopterin
-
A133S mutant enzyme; recombinant wild-type enzyme
0.0009
quinonoid dihydrobiopterin
-
Y146F mutant enzyme
0.001
quinonoid dihydrobiopterin
-
cofactor NADH
0.0025
quinonoid dihydrobiopterin
-
enzyme form III
0.0028
quinonoid dihydrobiopterin
-
enzyme form I
0.00285
quinonoid dihydrobiopterin
-
enzyme form II
0.007
quinonoid dihydrobiopterin
-
Y146H mutant enzyme
0.009
quinonoid dihydrobiopterin
-
cofactor NADPH
0.02
quinonoid dihydrobiopterin
-
A133S mutant enzyme
0.023
quinonoid dihydrobiopterin
-
Y146H mutant enzyme
0.024
quinonoid dihydrobiopterin
-
Y146F/A133S mutant enzyme
0.026
quinonoid dihydrobiopterin
-
K150I mutant enzyme
0.027
quinonoid dihydrobiopterin
-
recombinant wild-type enzyme
0.03
quinonoid dihydrobiopterin
-
D37I mutant enzyme
0.033
quinonoid dihydrobiopterin
-
K150Q mutant enzyme
0.039
quinonoid dihydrobiopterin
-
K150M mutant enzyme
0.041
quinonoid dihydrobiopterin
-
Y146F/K150Q double mutant enzyme
0.07
quinonoid dihydrobiopterin
-
W86I mutant enzyme
0.16
quinonoid dihydrobiopterin
-
-
0.226
quinonoid dihydrobiopterin
-
-
0.308
quinonoid dihydrobiopterin
-
Y146F mutant enzyme
1
quinonoid dihydrobiopterin
-
Y146F/K150E mutant enzyme, more than
1.32
Quinonoid dihydromonapterin
-
-
1.05
Quinonoid dihydroneopterin
-
-
1.45
quinonoid L-threo-dihydroneopterin
-
-
0.525
quinonoid-6,7-dimethyl-7,8-dihydropterin
-
-
0.128
quinonoid-6-methyl-7,8-dihydrobiopterin
-
-
0.0049
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant wild-type glutathione-S-transferase fusion enzyme
0.0062
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant G151S mutant enzyme
0.0181
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant wild-type enzyme
0.0819
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant Y150H mutant enzyme
0.0874
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant Y150H glutathione-S-transferase fusion mutant enzyme
0.0988
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant G23D mutant enzyme
0.149
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant Y150E glutathione-S-transferase fusion mutant enzyme
0.165
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant Y150F glutathione-S-transferase fusion mutant enzyme
0.283
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant Y150S mutant enzyme
0.33
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant Y150K glutathione-S-transferase fusion mutant enzyme
0.406
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant Y150S glutathione-S-transferase fusion mutant enzyme
0.434
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant Y150E mutant enzyme
0.48
quinonoid-6-methyl-7,8-dihydropterin
-
recombinant Y150F mutant enzyme
0.0009
quinonoid-7,8-dihydrobiopterin
-
recombinant wild-type enzyme
0.004
quinonoid-7,8-dihydrobiopterin
-
recombinant Y150H mutant enzyme
0.0305
quinonoid-7,8-dihydrobiopterin
-
recombinant Y150S mutant enzyme
0.0593
quinonoid-7,8-dihydrobiopterin
-
recombinant Y150F mutant enzyme
0.252
quinonoid-7,8-dihydrobiopterin
-
recombinant Y150E mutant enzyme
0.0009
quinonoid-7,8-dihydropterin
-
recombinant wild-type enzyme
0.0075
quinonoid-7,8-dihydropterin
-
recombinant G151S mutant enzyme
0.144
quinonoid-7,8-dihydropterin
-
recombinant G23D mutant enzyme
0.0034
quinonoid-dihydro-6-methylpterin
-
-
0.0009
tetrahydrobiopterin
-
cofactor NADPH
0.001
tetrahydrobiopterin
-
cofactor NADH
0.0011
tetrahydrobiopterin
-
-
0.0011
tetrahydrobiopterin
-
NADH-specific liver enzyme, cofactor NADPH
0.0016
tetrahydrobiopterin
-
NADH-specific liver enzyme, cofactor NADH
0.0068
tetrahydrobiopterin
-
NADPH-specific liver enzyme, cofactor NADPH
0.017
tetrahydrobiopterin
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
510
2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine
-
-
17
NADH
-
recombinant enzyme
43
NADH
-
D37I mutant enzyme
150
NADH
-
W104F mutant enzyme
156
NADH
-
native liver enzyme
158
NADH
-
recombinant liver enzyme
159
NADH
-
A6V mutant enzyme
280
NADH
-
enzyme from brain
20
NADPH
-
recombinant enzyme
162
quinoid 2-amino-4-hydroxy-6,7-dimethyl-7,8-dihydropteridine
-
recombinant enzyme
2
quinoid 6,7-dimethyldihydropteridine
-
Y146F/A133S mutant enzyme
17
quinoid 6,7-dimethyldihydropteridine
-
Y146F mutant enzyme
36
quinoid 6,7-dimethyldihydropteridine
-
Y146H mutant enzyme
52
quinoid 6,7-dimethyldihydropteridine
-
K150E mutant enzyme
152
quinoid 6,7-dimethyldihydropteridine
-
A133S mutant enzyme
153
quinoid 6,7-dimethyldihydropteridine
-
recombinant wild-type enzyme
0.3
quinoid 6-methyl-7,8-dihydropterin
-
recombinant G23D mutant enzyme
2.3
quinoid 6-methyl-7,8-dihydropterin
-
recombinant Y150E glutathione-S-transferase fusion mutant enzyme
6.7
quinoid 6-methyl-7,8-dihydropterin
-
recombinant Y150K glutathione-S-transferase fusion mutant enzyme
7.3
quinoid 6-methyl-7,8-dihydropterin
-
recombinant Y150E mutant enzyme
7.7
quinoid 6-methyl-7,8-dihydropterin
-
recombinant Y150F glutathione-S-transferase fusion mutant enzyme
15.3
quinoid 6-methyl-7,8-dihydropterin
-
recombinant Y150F mutant enzyme
31
quinoid 6-methyl-7,8-dihydropterin
-
recombinant wild-type glutathione-S-transferase fusion enzyme
35.8
quinoid 6-methyl-7,8-dihydropterin
-
recombinant Y150S mutant enzyme
42
quinoid 6-methyl-7,8-dihydropterin
-
recombinant Y150S glutathione-S-transferase fusion mutant enzyme
49.6
quinoid 6-methyl-7,8-dihydropterin
-
recombinant Y150H mutant enzyme
60
quinoid 6-methyl-7,8-dihydropterin
-
recombinant Y150H glutathione-S-transferase fusion mutant enzyme
107
quinoid 6-methyl-7,8-dihydropterin
-
recombinant G151S mutant enzyme
227
quinoid 6-methyl-7,8-dihydropterin
-
recombinant wild-type enzyme
16.7
quinoid 7,8-dihydrobiopterin
-
recombinant Y150E mutant enzyme
17
quinoid 7,8-dihydrobiopterin
-
recombinant enzyme
42.2
quinoid 7,8-dihydrobiopterin
-
recombinant Y150H mutant enzyme
44.5
quinoid 7,8-dihydrobiopterin
-
recombinant wild-type enzyme
50.3
quinoid 7,8-dihydrobiopterin
-
recombinant Y150S mutant enzyme
52.2
quinoid 7,8-dihydrobiopterin
-
recombinant Y150F mutant enzyme
15.7
quinoid 7,8-dihydropterin
-
recombinant G23D mutant enzyme
44.5
quinoid 7,8-dihydropterin
-
recombinant wild-type enzyme
51.2
quinoid 7,8-dihydropterin
-
recombinant G151S mutant enzyme
269
quinoid dihydrobiobiopterin
-
K150E mutant enzyme
1.7
quinoid dihydrobiopterin
-
Y146F mutant enzyme
20
quinoid dihydrobiopterin
-
A133S mutant enzyme
23
quinoid dihydrobiopterin
-
Y146H mutant enzyme
23
quinoid dihydrobiopterin
-
recombinant wild-type enzyme
26
quinoid dihydrobiopterin
-
K150M mutant enzyme
36
quinoid dihydrobiopterin
-
D37I mutant enzyme
64
quinoid dihydrobiopterin
-
K150I mutant enzyme; W86I mutant enzyme
74
quinoid dihydrobiopterin
-
Y146F/A133S mutant enzyme
76
quinoid dihydrobiopterin
-
Y146F/K150Q double mutant enzyme
90
quinoid dihydrobiopterin
-
K150Q mutant enzyme
138
quinoid dihydrobiopterin
-
Y146F mutant enzyme
139
quinoid dihydrobiopterin
-
Y146H mutant enzyme
149
quinoid dihydrobiopterin
-
A133S mutant enzyme
153
quinoid dihydrobiopterin
-
recombinant wild-type enzyme
200
quinoid dihydrobiopterin
-
Y146F/K150E mutant enzyme, approx. value
10.9
quinonoid 7,8(6H)-dihydropterin
-
at 20C
23.7
quinonoid 7,8(6H)-dihydropterin
-
at 25C
28.9
quinonoid 7,8(6H)-dihydropterin
-
30C
113
quinonoid 7,8(6H)-dihydropterin
-
at 37C
10.9
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 20C
23.7
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 25C
28.9
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 30C
113
quinonoid 7,8-(6H)-dihydrobiopterin
-
at 37C
20
quinonoid dihydrobiopterin
-
-
200
tetrahydrobiopterin
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
(R)-2,10,11-trihydroxyapomorphine
-
-
0.0012
(R)-apomorphine
-
-
0.0022
(R)-apomorphine
-
-
0.0013
(R)-N-n-propylaporphine
-
-
0.0022
(R)-N-n-propylaporphine
-
-
0.0028
1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine
-
noncompetitive inhibition
0.023
2,4-diamino-7,8-dihydropteroylglutamic acid
-
-
0.0295
2,4-diaminopteroic acid
-
-
0.024
2,4-diaminopteroylglutamic acid
-
-
0.014
3',4'-deoxynorlaudanosoline-carboxylic acid
-
vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.031
3',4'-deoxynorlaudanosoline-carboxylic acid
-
vs. NADH
0.0037
3-(4-hydroxyphenyl)pyruvate
-
-
0.024
6-Hydroxydopamine
-
noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine and NADH
0.0049
Adrenochrome
-
-
0.01
aminopterin
-
noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.011
aminopterin
-
noncompetitive vs. NADH
0.21
aminopterin
-
-
0.006
dopamine
-
vs. NADH
0.0065
dopamine
-
vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.007
dopamine
-
noncompetitive vs. NADH
0.014
dopamine
-
noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.11
epinephrine
-
noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.14
epinephrine
-
noncompetitive vs. NADH
0.0015
higenamine
-
vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.0023
higenamine
-
vs. NADH
0.0045
higenamine-1-carboxylic acid
-
vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.26
L-Dopa
-
-
0.016
L-thyroxine
-
-
0.25
L-tyrosine
-
-
0.067
m-tyramine
-
-
0.025
methotrexate
-
-
0.038
methotrexate
-
-
0.26
methotrexate
-
-
0.0032
NADP+
-
NADPH-specific enzyme
0.0032
NADP+
-
-
0.49
noradrenaline
-
noncompetitive inhibition
0.016
norepinephrine
-
noncompetitive vs. NADH
0.19
norepinephrine
-
noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
1
phenylalanine
-
mixed inhibition
1
Phenyllactate
-
mixed inhibition
0.05
phenylpyruvate
-
mixed inhibition
0.01
phenylpyruvic acid
-
uncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.022
quinonoid 2,4-diamino-7,8-dihydropteroylglutamic acid
-
-
0.09
salsolinol
-
-
1.2
serotonin
-
competitive inhibition
0.2
tryptophan
-
mixed inhibition
0.024
tyramine
-
noncompetitive vs. NADH
0.05
tyramine
-
-
0.05
tyramine
-
noncompetitive vs. quinonoid 2-amino-6,7-dimethyl-4-hydroxydihydropteridine
0.074
[4-hydroxyphenyl]acetic acid
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
tyramine
-
IC50: 0.04 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.069
Q8WTJ2
enzyme extract of microplasmodia
0.431
-
NADPH-specific enzyme from liver
0.706
-
NADPH-specific liver enzyme
0.972
-
NADPH-specific enzyme
0.972
-
NADPH-specific liver enzyme
2.51
-
-
5.2
-
recombinant enzyme, substrate dihydrofolate
20.2
-
NADH-specific liver enzyme
24
-
NADH-specific liver enzyme
26.2
-
NADH-specific liver enzyme
26.2
-
recombinant enzyme, substrate 6,7-dimethyl-7,8-dihydropteridine
38.3
Q8WTJ2
purified recombinant enzyme
56
-
T119 insert mutant enzyme
70.7
-
NADH-specific enzyme
70.7
-
-
125.8
-
recombinant enzyme
224
-
enzyme from brain
300
-
W104G mutant enzyme
412
-
recombinant enzyme
610
-
enzyme from brain
800
-
recombinant enzyme
1180
-
enzyme from brain
additional information
-
0.00205 mmol/min/0.001 ml liver extract, cofactor NADH, 0.00008 mmol/min/0.001 ml liver extract, cofactor NADPH
additional information
-
0.00261 mmol/min/0.001 ml liver extract, cofactor NADH, 0.00007 mmol/min/0.001 ml liver extract, cofactor NADPH
additional information
-
0.00264 mmol/min/0.001 ml liver extract, cofactor NADH, 0.00006 mmol/min/0.001 ml liver extract, cofactor NADPH; 0.0027 mmol/min/0.001 ml liver extract, cofactor NADH, 0.0001 mmol/min/0.001 ml liver extract, cofactor NADPH
additional information
-
0.0013 mmol/min/0.001 ml liver extract, cofactor NADH, 0.00009 mmol/min/0.001 ml liver extract, cofactor NADPH
additional information
-
-
additional information
-
0.003359 micromol reduced cytochrome c/min/5 mm disc, activity in blood of healty volunteers
additional information
Q8WTJ2
-
additional information
-
dihydropteridine reductase activity is reduced in 5-week-old (-11.8fold), 8-week-old (-18.4fold), and 13-week-old (-37.4fold) hypertensive rats compared to normotensive rats
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
-
assay at
7
-
recombinant wild-type, D37I, W86I, Y146F, Y146H, K150Q, K150I, K150M, N186A, A133S and Y146F/K150Q mutant enzymes
7.5
-
assay at
7.6
-
NADH-specific liver enzyme
7.6
P09417
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 7.8
-
pH 6.8: about 45% activity, pH 7.8: about 15% activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
P09417
assay at
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 4.7
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24600
-
calculated, monomer
695339
25000
-
SDS-PAGE, monomer
695339
41000
-
gradient PAGE
484958, 484995
43500 - 49000
-
gel filtration
484963
46000
Q8WTJ2
about, recombinant enzyme, gel filtration
654920
47000
-
gel filtration
484962
47500
-
gel filtration
484961
47500
-
-
484993
49000 - 50000
-
NADH-dihydropteridine reductase
484959
49000
-
sedimentation equilibrium analysis
484971
49000
-
-
484989
49000
-
NADH-specific liver enzyme, gel filtration
484989
50000
-
sedimentation equilibrium
484961
50000
-
-
484993
50000
-
gel-filtration chromatography (Superdex 200 column), dimer
695339
51000
-
gel filtration
484998
54000
-
gradient PAGE
484961, 484993
54000
-
gel filtration
484997
55000
-
gel filtration
484992
65000
-
equilibrium centrifugation, NADPH-specific liver enzyme
484960, 484999
68000
-
NADPH-specific enzyme, gel filtration
484960, 484999
69000
-
NADPH-specific liver enzyme, gel filtration
484999
70000
-
NADPH-specific enzyme, native PAGE
484960
70000
-
gradient PAGE
484994
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 24528, deduced from nuclotide sequence
dimer
-
-
dimer
-
-
dimer
-
2 * 27000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
homodimer
dimer
-
2 * 25500, SDS-PAGE, alpha,alpha, 2 * 25500, alpha,beta, 2 * 25500, beta,beta, 2 * 25500, 2 distinct subunits alpha and beta identified, the forms I, II and III represent three different dimeric combinations, SDS-PAGE
dimer
-
2 * 25774, deduced from nucleotide sequence
dimer
-
2 * 25420, deduced from nucleotide sequence
dimer
-
2 * 35000, NADPH-specific liver enzyme, SDS-PAGE
dimer
-
2 * 21000, liver, SDS-PAGE
dimer
-
2 * 25000, NADH-specific liver enzyme, SDS-PAGE
dimer
-
2 * 27000
dimer
-
2 * 27000, brain, SDS-PAGE
dimer
-
2 * 25000, NADH-dihydropteridine reductase
dimer
-
2 * 35000, NADPH-specific dihydropteridine reductase, SDS-PAGE
dimer
Q8WTJ2
2 * 23000, about, recombinant enzyme, SDS-PAGE
oligomer
-
x * 23000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 25000, four molecules form 2 dimers in the asymmetric unit in crystals
additional information
-
x * 25000, SDS-PAGE, weak band at 50000 Da which possibly corresponds to the dimeric form of the enzyme, calculated mass of the His-tagged protein is 24200 Da
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
silky crystals in the presence or absence of NADH upon a slow increase of ammonium sulfate concentration up to 50-55% at pH 6.5
-
complexed with NAD+, hanging drop vapor diffusion method, using 17% (w/v) polyethylene glycol 3350 and 100 mM Bis-Tris at pH 6.5
Q86A17
dicDHPR-NAD complex by incubation in 20 mM Tris-HCl, pH 8.0, hanging-drop vapor diffusion (4 microl drops), 18C (291 K), screening solution (0.1 M bis-tris, pH 6.5, 17% PEG 3350), hexahistidine tag not removed, x-ray diffraction
-
hanging drop vapour diffusion, polyethylene glycol 4500, various concentrations of Tris phosphate buffer, pH 7.8, 8% methanol and 1 mM beta-mercaptoethanol, 2.5 A resolution
-
hanging drop vapour diffusion, 2 crystal forms depending on whether inorganic salts or alcohols are used as precipitating agents, crystals diffract to at least 2.3 A
-
hanging drop vapour diffusion, polyethylene glycol 4500, Tris phosphate, pH 7.8, 10% methanol, 4C, crystals of binary complexes with NADH of recombinant wild-type, W86I, Y146F, Y146H, Y146F/K150Q and A133S mutant enzymes, 2.1-2.3 A resolution
-
selenomethionine-substitued enzyme in complex with inhibitor methotrexate or substrate dihydrofolate
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
unstable below and above
484992
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
5 min, 80% loss of activity, EDTA protects
484963
80
-
1 min, inactivation
484990
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
not stable during gel filtration
-
unstable to (NH4)2SO4 precipitation
-
NADH protects against inactivation
-
NADPH protects against inactivation
-
stable to freezing at -70C and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, stable for at least 2 years
-
-80C, stable for at least 3 months
-
-80C, 40 mM potassium phosphate buffer, pH 6.8, stable for at least a week
-
-80C, stable for years
-
-20C, stable for at least a year, enzyme activity in ammonium sulfate precipitate
-
4C, stable for up to 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
simple two step procedure i.e. affinity chromatography on Matrex gel blue A and hydrophobic chromatography on phenyl-Sepharose
-
cells centrifuged, washed with PBS (pH 7.4), resuspended in lysis buffer (50 mM Tris-HCl, pH 7.5), disrupted by sonication, centrifugation, supernatant filtered (0.45 microm), applied to a column with nickel-NTA beads, eluted (50 mM Tris-HCl, pH 7.5), active fractions pooled, concentrated, and exchanged into 50 mM sodium phosphate, pH 6.8, ultrafiltration, applied to a cation-exchange chromatography HS20 column, eluted with salt gradient at pH 6.8, concentration by ultrafiltration, gel-filtration chromatography with Superdex 200 column in 50 mM Tris-HCl, pH 8.0, concentration of eluted fractions in 20 mM Tris-HCl, pH 8.0, by ultrafiltration
-
nickel-affinity column chromatography
Q86A17
recombinant enzyme
-
naphthoquinone affinity chromatography, 5'-AMP-Sepharose
-
recombinant wild-type, G19D, W104G and T119insert mutant enzymes
-
simple two step procedure i.e. affinity chromatography on Matrex gel blue A and hydrophobic chromatography on phenyl-Sepharose
-
wild-type and recombinant Y150H, Y150S, Y150F, Y150E, Y150K, G151S and G23D mutant enzymes
-
recombinant enzyme from Escherichia coli by ion exchange chromatography and gel filtration to homogeneity
Q8WTJ2
ATCC 11299a
-
homogenization of smooth muscle strips in 2-DE lysis buffer containing 8 M urea, 2 M thiourea, 65 mM DTT, 2% CHAPS, and protease inhibitor cocktail, centrifugation, supernatant used for 2-DE and MALDI-TOF/TOF-MS
-
native enzyme and recombinant wild-type, W104F, A6V and D37I mutant enzyme
-
recombinant wild-type and several mutant enzymes
-
simple two step procedure i.e. affinity chromatography on Matrex gel blue A and hydrophobic chromatography on phenyl-Sepharose
-
recombinant protein using His-tag
-
recombinant enzyme, partially from Escherichia coli, solubilization at pH 10.0
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dicDHPR gene (residues 1-231) cloned into pET-28b expression plasmid with hexahistidine tag and thrombin cleavage site, expression in Escherichia coli BL21 (DE3)
-
expression of cloned cDNA in Escherichia coli
-
cloning of full-length cDNA, expression in COS cells
-
expression of wild-type, G19D, W104G and T119insert mutant enzymes in Escherichia coli
-
expression of wild-type, Y150H, Y150S, Y150F, Y150E, Y150K, G151S and G23D in Escherichia coli
-
high-level expression in Escherichia coli
-
recombinant expression in Escherichia coli
Q8WTJ2
expressed in HEK-293T cells
-
expression of wild-type and several mutants in Escherichia coli
-
liver enzyme expressed in Escherichia coli
-
expressed as His-tag fusion protein in Escherichia coli
-
DNA sequence determination and analysis, overexpression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is significantly decreased in the renal cortex of diabetic rats
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G151S
-
mutation found in children suffering from phenylketonuria due to enzyme deficiency
G19D
-
completely inactive
G23D
-
mutation found in children suffering from phenylketonuria due to enzyme deficiency, inactive mutant enzyme
T119insert
-
reduced activity
W104G
-
similar activity as wild-type
Y150E
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
Y150F
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
Y150H
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
Y150K
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
Y150S
-
lower kcat with 6-methyl-7,8-dyhydropterin than wild-type
A133S
-
similar kcat for quinonoid dihydrobiopterin as wild-type
A6V
-
no significant differences to wild-type
D37I
-
significant lower kcat
D37I
-
lower kcat for quinonoid dihydrobiopterin than wild-type
K150I
-
lower kcat for quinonoid dihydrobiopterin than wild-type
K150M
-
lower kcat for quinonoid dihydrobiopterin than wild-type
K150Q
-
lower kcat for quinonoid dihydrobiopterin than wild-type
N186A
-
lower kcat for quinonoid dihydrobiopterin than wild-type
W104F
-
no significant differences to wild-type
W86I
-
lower kcat for quinonoid dihydrobiopterin than wild-type
Y146F
-
2 orders of magnitude lower kcat than the wild-type enzyme
Y146F
-
almost no activity with quinonoid dihydrobipterin
Y146F/A133S
-
almost no activity with quinonoid 6,7-dimethyldihydropteridine, higher activity with quinoid dihydrobipterin than wild-type
Y146F/K150E
-
no activity with quinonoid 6,7-dimethyldihydropteridine, higher activity with quinoid dihydrobipterin than wild-type
Y146F/K150Q
-
lower kcat for quinonoid dihydrobiopterin than wild-type
Y146H
-
lower kcat for quinonoid dihydrobiopterin than wild-type
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
enzyme deficiency leads to progressive mental and physical retardation despite dietary phenylalanine restriction. Overview on genomic structure and location of natural mutations in the QDPR gene coding for enzyme